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Proteolytic cleavage of bacteriophage lambda repressor in induction.

J W Roberts, C W Roberts

    Proceedings of the National Academy of Sciences of the United States of America
    |January 1, 1975
    PubMed
    Summary
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    Bacteriophage lambda repressor cleavage, essential for lysogenic state induction, is prevented by mutations in the repressor or recA gene. This suggests proteolytic cleavage may be the primary inactivation mechanism during induction.

    Area of Science:

    • Molecular Biology
    • Bacteriology
    • Genetics

    Background:

    • The bacteriophage lambda repressor protein maintains bacterial lysogeny.
    • Lysogenic induction involves repressor inactivation, often triggered by DNA damage.
    • Mitomycin C and UV light are common inducers of lambda phage lysogeny.

    Purpose of the Study:

    • To investigate the mechanism of bacteriophage lambda repressor inactivation during lysogenic induction.
    • To determine the role of proteolytic cleavage in repressor inactivation.
    • To explore the involvement of host factors, specifically the recA gene product, in this process.

    Main Methods:

    • Induction of lambda lysogens with mitomycin C or UV light.
    • Analysis of bacteriophage lambda repressor cleavage in response to induction.

    Related Experiment Videos

  • Genetic analysis using mutations in the phage repressor and the host recA gene.

    • Main Results:

    • Bacteriophage lambda repressor undergoes proteolytic cleavage upon induction by mitomycin C or UV light.
    • Mutational alterations in the phage repressor or the host recA gene prevent repressor cleavage.
    • This indicates that repressor cleavage is dependent on functional repressor and recA gene product.

    Conclusions:

    • Proteolytic cleavage is a key event in the inactivation of the bacteriophage lambda repressor during lysogenic induction.
    • The recA gene product plays a crucial role in the pathway leading to repressor cleavage.
    • Repressor inactivation may be primarily mediated by proteolytic cleavage or a subsequent event.